Abstract
The fifth order processes to the signals of ultrafast infrared spectrally resolved stimulated vibrational echoes were investigated in carbonmonoxy heme proteins. It was stated that the fifth order effects of spectrally resolved vibrational echoes arose at 1-0 and the 2-1 emission frequencies of the stretching mode of the CO chromophore bound at the active site of heme proteins. Fifth order Feynman diagrams analysis demonstrated the reason for the greater influence of fifth order processes on the 1-2 transition. It was found that the anharmonic oscillations in vibrational echo data of hemoglobin carbonmonoxy arises even without fifth order contributions.
Original language | English |
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Pages (from-to) | 877-885 |
Number of pages | 9 |
Journal | Journal of Chemical Physics |
Volume | 121 |
Issue number | 2 |
DOIs | |
State | Published - 8 Jul 2004 |